CYGB1_DANRE
ID CYGB1_DANRE Reviewed; 174 AA.
AC Q8UUR3; Q504J2;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cytoglobin-1;
GN Name=cygb1; Synonyms=cygb, cygb-1; ORFNames=zgc:109806;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11919282; DOI=10.1093/oxfordjournals.molbev.a004096;
RA Burmester T., Ebner B., Weich B., Hankeln T.;
RT "Cytoglobin: a novel globin type ubiquitously expressed in vertebrate
RT tissues.";
RL Mol. Biol. Evol. 19:416-421(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Larva;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=16199220; DOI=10.1016/j.bbrc.2005.08.271;
RA Fuchs C., Luckhardt A., Gerlach F., Burmester T., Hankeln T.;
RT "Duplicated cytoglobin genes in teleost fishes.";
RL Biochem. Biophys. Res. Commun. 337:216-223(2005).
CC -!- FUNCTION: May have a protective function during conditions of oxidative
CC stress. May be involved in intracellular oxygen storage or transfer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined with highest
CC levels in brain, eye, gut and heart. {ECO:0000269|PubMed:16199220}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; AJ320232; CAC86225.1; -; mRNA.
DR EMBL; BC094999; AAH94999.1; -; mRNA.
DR RefSeq; NP_694484.1; NM_152952.2.
DR AlphaFoldDB; Q8UUR3; -.
DR SMR; Q8UUR3; -.
DR STRING; 7955.ENSDARP00000055793; -.
DR PaxDb; Q8UUR3; -.
DR GeneID; 246090; -.
DR KEGG; dre:246090; -.
DR CTD; 246090; -.
DR ZFIN; ZDB-GENE-020513-1; cygb1.
DR eggNOG; KOG3378; Eukaryota.
DR InParanoid; Q8UUR3; -.
DR OrthoDB; 1379813at2759; -.
DR PhylomeDB; Q8UUR3; -.
DR PRO; PR:Q8UUR3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0098809; F:nitrite reductase activity; IDA:ZFIN.
DR GO; GO:0019825; F:oxygen binding; IDA:ZFIN.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR GO; GO:0046686; P:response to cadmium ion; IEP:ZFIN.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR013314; Globin_lamprey/hagfish.
DR PANTHER; PTHR46783; PTHR46783; 1.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR01906; FISHGLOBIN.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Heme; Iron; Metal-binding; Oxygen transport; Reference proteome;
KW Transport.
FT CHAIN 1..174
FT /note="Cytoglobin-1"
FT /id="PRO_0000053387"
FT REGION 14..165
FT /note="Globin"
FT BINDING 78
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 110
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT CONFLICT 77
FT /note="E -> K (in Ref. 1; CAC86225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 19909 MW; DAAF8924E7468ECA CRC64;
MEGDGGVQLT QSPDSLTEED VCVIQDTWKP VYAERDNAGV AVLVRFFTNF PSAKQYFEHF
RELQDPAEMQ QNAQLKEHGQ RVLNALNTLV ENLRDADKLN TIFNQMGKSH ALRHKVDPVY
FKILAGVILE VLVEAFPQCF SPAEVQSSWS KLMGILYWQM NRVYAEVGWE NSKK